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CAZyme Information: MGYG000003948_01100

You are here: Home > Sequence: MGYG000003948_01100

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species
Lineage Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes;
CAZyme ID MGYG000003948_01100
CAZy Family GH29
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
475 53193.72 4.6444
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000003948 2150232 MAG United Kingdom Europe
Gene Location Start: 24327;  End: 25754  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

EC 3.2.1.111 3.2.1.51

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH29 38 344 4.7e-80 0.838150289017341

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG3669 AfuC 2.64e-61 25 458 6 413
Alpha-L-fucosidase [Carbohydrate transport and metabolism].
pfam01120 Alpha_L_fucos 6.50e-44 59 340 69 321
Alpha-L-fucosidase.
smart00812 Alpha_L_fucos 3.89e-39 70 350 76 336
Alpha-L-fucosidase. O-Glycosyl hydrolases (EC 3.2.1.-) are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site. Because the fold of proteins is better conserved than their sequences, some of the families can be grouped in 'clans'. Family 29 encompasses alpha-L-fucosidases, which is a lysosomal enzyme responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. Deficiency of alpha-L-fucosidase results in the lysosomal storage disease fucosidosis.
pfam00754 F5_F8_type_C 7.22e-04 361 462 2 114
F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BBE17422.1 8.77e-186 14 475 16 485
AXE20758.1 4.13e-184 25 475 350 806
ANH83611.1 1.44e-182 11 475 16 487
AEI46547.1 7.51e-182 25 475 350 806
SOE20179.1 1.64e-179 12 475 39 509

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5K9H_A 5.65e-127 27 475 34 463
Crystalstructure of a glycoside hydrolase 29 family member from an unknown rumen bacterium [unidentified]
4ZRX_A 1.41e-107 30 475 30 458
Crystalstructure of a putative alpha-L-fucosidase (BACOVA_04357) from Bacteroides ovatus ATCC 8483 at 1.59 A resolution [Bacteroides ovatus ATCC 8483]
3UES_A 7.70e-104 29 473 16 474
Crystalstructure of alpha-1,3/4-fucosidase from Bifidobacterium longum subsp. infantis complexed with deoxyfuconojirimycin [Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088],3UES_B Crystal structure of alpha-1,3/4-fucosidase from Bifidobacterium longum subsp. infantis complexed with deoxyfuconojirimycin [Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088]
3UET_A 9.60e-102 29 473 16 474
Crystalstructure of alpha-1,3/4-fucosidase from Bifidobacterium longum subsp. infantis D172A/E217A mutant complexed with lacto-N-fucopentaose II [Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088],3UET_B Crystal structure of alpha-1,3/4-fucosidase from Bifidobacterium longum subsp. infantis D172A/E217A mutant complexed with lacto-N-fucopentaose II [Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088]
3MO4_A 1.44e-101 29 473 18 476
Thecrystal structure of an alpha-(1-3,4)-fucosidase from Bifidobacterium longum subsp. infantis ATCC 15697 [Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088],3MO4_B The crystal structure of an alpha-(1-3,4)-fucosidase from Bifidobacterium longum subsp. infantis ATCC 15697 [Bifidobacterium longum subsp. infantis ATCC 15697 = JCM 1222 = DSM 20088]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
Q8GW72 1.96e-108 25 475 31 477
Alpha-L-fucosidase 1 OS=Arabidopsis thaliana OX=3702 GN=FUC1 PE=1 SV=2
Q7XUR3 1.86e-102 25 475 33 476
Putative alpha-L-fucosidase 1 OS=Oryza sativa subsp. japonica OX=39947 GN=Os04g0560400 PE=3 SV=2
Q6AYS4 9.71e-13 39 350 70 358
Plasma alpha-L-fucosidase OS=Rattus norvegicus OX=10116 GN=Fuca2 PE=2 SV=1
Q9BTY2 1.32e-12 69 350 106 366
Plasma alpha-L-fucosidase OS=Homo sapiens OX=9606 GN=FUCA2 PE=1 SV=2
P49713 1.38e-12 70 350 92 348
Putative alpha-L-fucosidase OS=Caenorhabditis elegans OX=6239 GN=W03G11.3 PE=3 SV=2

SignalP and Lipop Annotations help

This protein is predicted as LIPO

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
0.000000 0.000003 1.000043 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000003948_01100.